(data stored in SCRATCH3701 zone)

SWISSPROT: MURC_RICTY

ID   MURC_RICTY              Reviewed;         498 AA.
AC   Q68XC2;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 95.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00046};
DE            EC=6.3.2.8 {ECO:0000255|HAMAP-Rule:MF_00046};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000255|HAMAP-Rule:MF_00046};
GN   Name=murC {ECO:0000255|HAMAP-Rule:MF_00046}; OrderedLocusNames=RT0239;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) +
CC         phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine;
CC         Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757,
CC         ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00046};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00046}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00046}.
DR   EMBL; AE017197; AAU03720.1; -; Genomic_DNA.
DR   RefSeq; WP_011190705.1; NC_006142.1.
DR   SMR; Q68XC2; -.
DR   STRING; 257363.RT0239; -.
DR   EnsemblBacteria; AAU03720; AAU03720; RT0239.
DR   KEGG; rty:RT0239; -.
DR   eggNOG; ENOG4105DFU; Bacteria.
DR   eggNOG; COG0773; LUCA.
DR   HOGENOM; HOG000256031; -.
DR   KO; K01924; -.
DR   OMA; DITYQLR; -.
DR   OrthoDB; 307881at2; -.
DR   BioCyc; RTYP257363:G1G0L-243-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   HAMAP; MF_00046; MurC; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_MurC.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR01082; murC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q68XC2.
DR   SWISS-2DPAGE; Q68XC2.
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..498
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_0000182144"
FT   NP_BIND         120..126
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   498 AA;  55048 MW;  A940C0D6AD10D1A1 CRC64;
     MLLLELKKTN QTLGTIHFIG IGGVGMSGIA EILHNLGYKV QGSDLVENYN TKRLESYGIK
     IFLGHAKQNI KNVSYVVISS AIHQNNPEIK EALERKIPII RRAEMLAELM RLKCSVAVSG
     SHGKTTTTSL IACLFEAAGL YPTVINGGII NNKSTNAYLG SSNYLIAEAD ESDATFIHIP
     STIAIITNID PEHLDYYQDF EILIGAFRSF ITNLPFYGFA VCCIDHKIVR KLVDDITERK
     IITYGIDAED AHIIAFNINT DIASSTFDVK ISLPNVLGTT IIEKITIPTP GRHNILNSLA
     AIAVGIELDF GIKAIKNGFN NFKGVKRRFT KVAEYNQAVI IDDYAHHPEE IKATLATAKN
     IANQQNGKVI AIFQPHRYSR IKYLFDDFML CFADADILYI TNIYAAGEKP IEGITGQSLV
     DKMTQNKYHD KANFLAELDD VVSVIIDHAA SGDMIIMMGA GNISSFANEL DRRLLSQEIL
     ASSQNTDFDT SSYDKVIR
//

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